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- PDB-1myl: SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1myl | ||||||
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Title | SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY | ||||||
![]() | ARC REPRESSOR | ||||||
![]() | TRANSCRIPTION REGULATION / HYPERSTABLE MUTANT | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schildbach, J.F. / Waldburger, C.D. / Sauer, R.T. | ||||||
![]() | ![]() Title: Are buried salt bridges important for protein stability and conformational specificity? Authors: Waldburger, C.D. / Schildbach, J.F. / Sauer, R.T. #1: ![]() Title: DNA Recognition by Beta-Sheets in the Arc Repressor-Operator Crystal Structure Authors: Raumann, B.E. / Rould, M.A. / Pabo, C.O. / Sauer, R.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.6 KB | Display | ![]() |
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PDB format | ![]() | 47.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 394.8 KB | Display | ![]() |
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Full document | ![]() | 398.9 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 10.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 6202.298 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.24 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 49.5 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 11168 / % possible obs: 90.8 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. measured all: 20111 / Rmerge(I) obs: 0.062 |
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Processing
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Refinement | Resolution: 2.4→6 Å / σ(F): 0
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Displacement parameters | Biso mean: 33.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.209 / Rfactor Rfree: 0.293 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.55 |